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In Situ Investigation on the Protein Corona Formation of Quantum Dots by Using Fluorescence Resonance Energy Transfer
Author(s) -
Qu Shaohua,
Sun Fangying,
Qiao Zihan,
Li Juanmin,
Shang Li
Publication year - 2020
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.201907633
Subject(s) - förster resonance energy transfer , quantum dot , circular dichroism , nanomaterials , nanoparticle , protein adsorption , chirality (physics) , electron paramagnetic resonance , human serum albumin , chemistry , fluorescence , materials science , adsorption , biophysics , nanotechnology , photochemistry , crystallography , nuclear magnetic resonance , chromatography , physics , chiral symmetry breaking , quantum mechanics , quark , nambu–jona lasinio model , biology
A fundamental understanding of nanoparticle–protein corona and its interactions with biological systems is essential for future application of engineered nanomaterials. In this work, fluorescence resonance energy transfer (FRET) is employed for studying the protein adsorption behavior of nanoparticles. The adsorption of human serum albumin (HSA) onto the surface of InP@ZnS quantum dots (QDs) with different chirality ( d ‐ and l ‐penicillamine) shows strong discernible differences in the binding behaviors including affinity and adsorption orientation that are obtained upon quantitative analysis of FRET data. Circular dichroism spectroscopy further confirms the differences in the conformational changes of HSA upon interaction with d ‐ and l ‐chiral QD surfaces. Consequently, the formed protein corona on chiral surfaces may affect their following biological interactions, such as possible protein exchange with serum proteins plasma as well as cellular interactions. These results vividly illustrate the potential of the FRET method as a simple yet versatile platform for quantitatively investigating biological interactions of nanoparticles.